HEADER ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 24-JUN-91 2HIP 2HIP 2 COMPND HIGH POTENTIAL IRON SULFUR PROTEIN (HI/PIP$) 2HIP 3 SOURCE (ECTOTHIORHODOSPIRA $HALOPHILA), A PURPLE PHOTOSYNTHETIC 2HIP 4 SOURCE 2 BACTERIUM 2HIP 5 AUTHOR D.R.BREITER,T.E.MEYER,I.RAYMENT,H.M.HOLDEN 2HIP 6 REVDAT 1 15-JUL-92 2HIP 0 2HIP 7 JRNL AUTH D.R.BREITER,T.E.MEYER,I.RAYMENT,H.M.HOLDEN 2HIP 8 JRNL TITL THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL 2HIP 9 JRNL TITL 2 IRON-*SULFUR PROTEIN ISOLATED FROM 2HIP 10 JRNL TITL 3 ECTOTHIORHODOSPIRA $HALOPHILA DETERMINED AT 2HIP 11 JRNL TITL 4 2.5-*ANGSTROMS RESOLUTION 2HIP 12 JRNL REF J.BIOL.CHEM. V. 266 18660 1991 2HIP 13 JRNL REFN ASTM JBCHA3 US ISSN 0021-9258 071 2HIP 14 REMARK 1 2HIP 15 REMARK 2 2HIP 16 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 2HIP 17 REMARK 3 2HIP 18 REMARK 3 REFINEMENT. BY USE OF THE RESTRAINED LEAST-SQUARES PACKAGE 2HIP 19 REMARK 3 (*TNT*) OF L. F. TEN EYCK AND D. E. TRONRUD. THE R-VALUE 2HIP 20 REMARK 3 IS 0.184. THE RMS DEVIATION FROM IDEALITY OF THE BOND 2HIP 21 REMARK 3 LENGTHS IS 0.014 ANGSTROMS. THE RMS DEVIATION FROM 2HIP 22 REMARK 3 IDEALITY OF THE BOND ANGLES IS 2.221 DEGREES. THE RMS 2HIP 23 REMARK 3 DEVIATION FROM IDEALITY OF THE PLANARITY (TRIGONAL) IS 2HIP 24 REMARK 3 0.003 ANGSTROMS. THE RMS DEVIATION FROM IDEALITY OF THE 2HIP 25 REMARK 3 PLANARITY (OTHER PLANES) IS 0.007 ANGSTROMS. THE RMS 2HIP 26 REMARK 3 DEVIATION FROM IDEALITY OF THE TORSION ANGLES IS 19.437 2HIP 27 REMARK 3 DEGREES. 2HIP 28 SEQRES 1 A 72 GLU PRO ARG ALA GLU ASP GLY HIS ALA HIS ASP TYR VAL 2HIP 29 SEQRES 2 A 72 ASN GLU ALA ALA ASP ALA SER GLY HIS PRO ARG TYR GLN 2HIP 30 SEQRES 3 A 72 GLU GLY GLN LEU CYS GLU ASN CYS ALA PHE TRP GLY GLU 2HIP 31 SEQRES 4 A 72 ALA VAL GLN ASP GLY TRP GLY ARG CYS THR HIS PRO ASP 2HIP 32 SEQRES 5 A 72 PHE ASP GLU VAL LEU VAL LYS ALA GLU GLY TRP CYS SER 2HIP 33 SEQRES 6 A 72 VAL TYR ALA PRO ALA SER SER 2HIP 34 SEQRES 7 B 72 GLU PRO ARG ALA GLU ASP GLY HIS ALA HIS ASP TYR VAL 2HIP 35 SEQRES 8 B 72 ASN GLU ALA ALA ASP ALA SER GLY HIS PRO ARG TYR GLN 2HIP 36 SEQRES 9 B 72 GLU GLY GLN LEU CYS GLU ASN CYS ALA PHE TRP GLY GLU 2HIP 37 SEQRES 10 B 72 ALA VAL GLN ASP GLY TRP GLY ARG CYS THR HIS PRO ASP 2HIP 38 SEQRES 11 B 72 PHE ASP GLU VAL LEU VAL LYS ALA GLU GLY TRP CYS SER 2HIP 39 SEQRES 12 B 72 VAL TYR ALA PRO ALA SER SER 2HIP 40 HET FS4 A 73 8 FE4-S4 CLUSTER 2HIP 41 HET FS4 B 73 8 FE4-S4 CLUSTER 2HIP 42 FORMUL 3 FS4 FE4 S4 2HIP 43 FORMUL 4 FS4 FE4 S4 2HIP 44 FORMUL 5 HOH *104(H2 O1) 2HIP 45 CRYST1 60.000 31.940 40.270 90.00 100.50 90.00 P 21 4 2HIP 46 ORIGX1 1.000000 0.000000 0.000000 0.00000 2HIP 47 ORIGX2 0.000000 1.000000 0.000000 0.00000 2HIP 48 ORIGX3 0.000000 0.000000 1.000000 0.00000 2HIP 49 SCALE1 0.016667 0.000000 0.003089 0.00000 2HIP 50 SCALE2 0.000000 0.031309 0.000000 0.00000 2HIP 51 SCALE3 0.000000 0.000000 0.025255 0.00000 2HIP 52